NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|26339464|dbj|BAC33403|]
View 

unnamed protein product [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614797)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

EC:  2.1.-.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12504684|12826405

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-154 9.61e-17

Methyltransferase domain; This family appears to be a methyltransferase domain.


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.14  E-value: 9.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    52 VLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLdavltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVL------- 73

                          90       100
                  ....*....|....*....|...
gi 26339464   132 EEVTLRQVDRMLAEVGRVLQVGG 154
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-154 9.61e-17

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.14  E-value: 9.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    52 VLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLdavltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVL------- 73

                          90       100
                  ....*....|....*....|...
gi 26339464   132 EEVTLRQVDRMLAEVGRVLQVGG 154
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-159 3.39e-16

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 74.26  E-value: 3.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464  30 EWYGTYLELCEVLHkyIKPKEKVLVIGCGNSELSEQLYDVGYQdIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLE 109
Cdd:COG2226   6 ARYDGREALLAALG--LRPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLP 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 26339464 110 FPDATFQVVLDKGTLDAVltdeeevtlRQVDRMLAEVGRVLQVGGRYLCI 159
Cdd:COG2226  83 FPDGSFDLVISSFVLHHL---------PDPERALAEIARVLKPGGRLVVV 123
PRK08317 PRK08317
hypothetical protein; Provisional
 46-158 1.26e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 60.72  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464   46 IKPKEKVLVIGCGNSELSEQLYD-VGYQ-DIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFqvvldkgt 123
Cdd:PRK08317  17 VQPGDRVLDVGCGPGNDARELARrVGPEgRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF-------- 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 26339464  124 lDAVLTDEEEVTLRQVDRMLAEVGRVLQVGGRYLC 158
Cdd:PRK08317  89 -DAVRSDRVLQHLEDPARALAEIARVLRPGGRVVV 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-159 1.95e-09

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 54.36  E-value: 1.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464  51 KVLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERN-GSRRPHMSFLKMDMTQLEF-PDATFQVVLdkgtLDAVL 128
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaALLADNVEVLKGDAEELPPeADESFDVII----SDPPL 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 26339464 129 TDEEEVtlrqVDRMLAEVGRVLQVGGRYLCI 159
Cdd:cd02440  77 HHLVED----LARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-154 9.61e-17

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.14  E-value: 9.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    52 VLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLdavltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVL------- 73

                          90       100
                  ....*....|....*....|...
gi 26339464   132 EEVTLRQVDRMLAEVGRVLQVGG 154
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-159 3.39e-16

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 74.26  E-value: 3.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464  30 EWYGTYLELCEVLHkyIKPKEKVLVIGCGNSELSEQLYDVGYQdIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLE 109
Cdd:COG2226   6 ARYDGREALLAALG--LRPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLP 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 26339464 110 FPDATFQVVLDKGTLDAVltdeeevtlRQVDRMLAEVGRVLQVGGRYLCI 159
Cdd:COG2226  83 FPDGSFDLVISSFVLHHL---------PDPERALAEIARVLKPGGRLVVV 123
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 37-157 2.10e-12

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 63.11  E-value: 2.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464  37 ELCEVLHKYIKPKEKVLVIGCGNSELSEQLYDVGYqDIVNIDISEVVIKQMKERngSRRPHMSFLKMDMTQLEFPDATFQ 116
Cdd:COG2227  13 RLAALLARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGSFD 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 26339464 117 VVldkgTLDAVLTDeeevtLRQVDRMLAEVGRVLQVGGRYL 157
Cdd:COG2227  90 LV----ICSEVLEH-----LPDPAALLRELARLLKPGGLLL 121
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 53-158 2.93e-11

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.22  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    53 LVIGCGNSELSEQLYDVGYQdIVNIDISEVVIKQMKERNgsRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLDavltdee 132
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISPEMLELAREKA--PREGLTFVVGDAEDLPFPDNSFDLVLSSEVLH------- 70

                          90       100
                  ....*....|....*....|....*.
gi 26339464   133 evTLRQVDRMLAEVGRVLQVGGRYLC 158
Cdd:pfam08241  71 --HVEDPERALREIARVLKPGGILII 94
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 46-185 6.11e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 59.74  E-value: 6.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    46 IKPKEKVLVIGCGNSELSEQLYDVGYQD--IVNIDISEVVIKQMKER---NGSRRphMSFLKMDMTQLE--FPDATFQVV 118
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNaeVVGIDISEEAIEKARENaqkLGFDN--VEFEQGDIEELPelLEDDKFDVV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26339464   119 LDKGTLDAVlTDEEEVtlrqvdrmLAEVGRVLQVGGRYLCISLAQAHILKKAVGHFSREGWMVRAHQ 185
Cdd:pfam13847  79 ISNCVLNHI-PDPDKV--------LQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGA 136
PRK08317 PRK08317
hypothetical protein; Provisional
 46-158 1.26e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 60.72  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464   46 IKPKEKVLVIGCGNSELSEQLYD-VGYQ-DIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFqvvldkgt 123
Cdd:PRK08317  17 VQPGDRVLDVGCGPGNDARELARrVGPEgRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF-------- 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 26339464  124 lDAVLTDEEEVTLRQVDRMLAEVGRVLQVGGRYLC 158
Cdd:PRK08317  89 -DAVRSDRVLQHLEDPARALAEIARVLRPGGRVVV 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-159 1.95e-09

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 54.36  E-value: 1.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464  51 KVLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERN-GSRRPHMSFLKMDMTQLEF-PDATFQVVLdkgtLDAVL 128
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaALLADNVEVLKGDAEELPPeADESFDVII----SDPPL 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 26339464 129 TDEEEVtlrqVDRMLAEVGRVLQVGGRYLCI 159
Cdd:cd02440  77 HHLVED----LARFLEEARRLLKPGGVLVLT 103
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 37-150 1.46e-06

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 47.23  E-value: 1.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464  37 ELCEVLHkyIKPKEKVLVIGCGNSELSEQL---YDVgyqDIVNIDISEVVIKQMKERNGSR--RPHMSFLKMDMTQLEfP 111
Cdd:COG2230  42 LILRKLG--LKPGMRVLDIGCGWGGLALYLarrYGV---RVTGVTLSPEQLEYARERAAEAglADRVEVRLADYRDLP-A 115

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 26339464 112 DATFQVVLDKGTLDAVLTDEEEVTLRQVDRMLAEVGRVL 150
Cdd:COG2230 116 DGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 47-158 4.76e-05

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.99  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464   47 KPKEKVLVIGCGNSELSEQLY-DVGYQD-IVNIDISEVVIKQMKER--NGSRRPHMSFLKMDMTQLEFPDATFqvvldkg 122
Cdd:PRK00216  50 RPGDKVLDLACGTGDLAIALAkAVGKTGeVVGLDFSEGMLAVGREKlrDLGLSGNVEFVQGDAEALPFPDNSF------- 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 26339464  123 tlDAVltdeeevT----LRQV---DRMLAEVGRVLQVGGRYLC 158
Cdd:PRK00216 123 --DAV-------TiafgLRNVpdiDKALREMYRVLKPGGRLVI 156
PRK14968 PRK14968
putative methyltransferase; Provisional
 34-157 1.12e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.19  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464   34 TYLeLCEVLHkyIKPKEKVLVIGCGNSELSEQLYDVGyQDIVNIDISEVVIKQMKE---RNGSRRPHMSFLKMDMtqlef 110
Cdd:PRK14968  12 SFL-LAENAV--DKKGDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAVECAKCnakLNNIRNNGVEVIRSDL----- 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26339464  111 pdatFQVVlDKGTLDAVL-------TDEEE-------------VTLRQV-DRMLAEVGRVLQVGGRYL 157
Cdd:PRK14968  83 ----FEPF-RGDKFDVILfnppylpTEEEEewddwlnyalsggKDGREViDRFLDEVGRYLKPGGRIL 145
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 35-107 2.76e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 40.25  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    35 YLELCEVLHKYIKPKEKVLVI---GCGNSELSEQLYDVGYQ-DIVNIDISEVVIKQMKERNgsRR----PHMSFLKMDMT 106
Cdd:pfam13679   9 LAEFIAPLLKELLDENGPITIvdhGAGKGYLGFILYYLKYGvRVYGIDTRAELVEKANALA--QKlgfnKRMSFLEGTIA 86


                  .
gi 26339464   107 Q 107
Cdd:pfam13679  87 G 87
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 46-124 5.94e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 41.27  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464   46 IKPKEKVLVIGCG----NSELSEQlYDVgyqDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDK 121
Cdd:PLN02336 264 LKPGQKVLDVGCGigggDFYMAEN-FDV---HVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSR 339


                 ...
gi 26339464  122 GTL 124
Cdd:PLN02336 340 DTI 342
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 14-161 8.63e-03

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 37.02  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    14 ADYWEKFFQqRGKTAFEWYGTYLELCEVLHKY-IKPKEKVLVIGCGNSE----LSEQLYDVgyqdiVNIDISEVVIKQMK 88
Cdd:pfam05724   3 PDFWLKRWV-EGQTPFHQEGVNPLLVRHWDALkLPPGLRVLVPLCGKALdmvwLAEQGHFV-----VGVEISELAVEKFF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26339464    89 ERNGSRRP--------HMSFLKMDMTQLEFPDAT------FQVVLDKGTLDAVltdEEEVTLRQVDRMLaevgRVLQVGG 154
Cdd:pfam05724  77 AEAGLSPPitelsgfkEYSSGNISLYCGDFFTLPreelgkFDLIYDRAALCAL---PPEMRPRYAKQMY----ELLPPGG 149


                  ....*..
gi 26339464   155 RYLCISL 161
Cdd:pfam05724 150 RGLLITL 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH